6GIY

The baseplate complex from the type VI secretion system


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.30 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Biogenesis and structure of a type VI secretion baseplate.

Cherrak, Y.Rapisarda, C.Pellarin, R.Bouvier, G.Bardiaux, B.Allain, F.Malosse, C.Rey, M.Chamot-Rooke, J.Cascales, E.Fronzes, R.Durand, E.

(2018) Nat Microbiol 3: 1404-1416

  • DOI: https://doi.org/10.1038/s41564-018-0260-1
  • Primary Citation of Related Structures:  
    6GIY, 6GJ1, 6GJ3

  • PubMed Abstract: 

    To support their growth in a competitive environment and cause pathogenesis, bacteria have evolved a broad repertoire of macromolecular machineries to deliver specific effectors and toxins. Among these multiprotein complexes, the type VI secretion system (T6SS) is a contractile nanomachine that targets both prokaryotic and eukaryotic cells. The T6SS comprises two functional subcomplexes: a bacteriophage-related tail structure anchored to the cell envelope by a membrane complex. As in other contractile injection systems, the tail is composed of an inner tube wrapped by a sheath and built on the baseplate. In the T6SS, the baseplate is not only the tail assembly platform, but also docks the tail to the membrane complex and hence serves as an evolutionary adaptor. Here we define the biogenesis pathway and report the cryo-electron microscopy (cryo-EM) structure of the wedge protein complex of the T6SS from enteroaggregative Escherichia coli (EAEC). Using an integrative approach, we unveil the molecular architecture of the whole T6SS baseplate and its interaction with the tail sheath, offering detailed insights into its biogenesis and function. We discuss architectural and mechanistic similarities but also reveal key differences with the T4 phage and Mu phage baseplates.


  • Organizational Affiliation

    Laboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, UMR7255, Aix-Marseille Université - CNRS, Marseille, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TssF
A, B
587Escherichia coliMutation(s): 0 
Gene Names: EC55989_3322
UniProt
Find proteins for B7LFT7 (Escherichia coli (strain 55989 / EAEC))
Explore B7LFT7 
Go to UniProtKB:  B7LFT7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupB7LFT7
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
TssG366Escherichia coliMutation(s): 0 
Gene Names: EC55989_3321
UniProt
Find proteins for B7LFT6 (Escherichia coli (strain 55989 / EAEC))
Explore B7LFT6 
Go to UniProtKB:  B7LFT6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupB7LFT6
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
TssK
D, E, F, G, H
D, E, F, G, H, I
444Escherichia coliMutation(s): 0 
Gene Names: EC55989_3338
UniProt
Find proteins for B7LG64 (Escherichia coli (strain 55989 / EAEC))
Explore B7LG64 
Go to UniProtKB:  B7LG64
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupB7LG64
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.30 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONRELION
MODEL REFINEMENTPHENIX

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-10-17
    Type: Initial release
  • Version 1.1: 2018-10-24
    Changes: Data collection, Database references
  • Version 1.2: 2018-12-05
    Changes: Data collection, Database references
  • Version 1.3: 2019-12-18
    Changes: Other
  • Version 1.4: 2024-05-15
    Changes: Data collection, Database references